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P42321 (CATA_PROMI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase
EC=1.11.1.6
Gene names
Name:katA
OrganismProteus mirabilis
Taxonomic identifier584 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

NADP.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the catalase family.

Mass spectrometry

Molecular mass is 55643±5 Da from positions 1 - 484. Determined by ESI. Ref.1

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionOxidoreductase
Peroxidase
   PTMOxidation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Catalase
PRO_0000084992

Sites

Active site541
Active site1271
Metal binding3371Iron (heme axial ligand) Ref.2

Amino acid modifications

Modified residue531Methionine sulfone

Secondary structure

1 .................................................................................... 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42321 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: ADC25F3CB41F5C50

FASTA48455,614
        10         20         30         40         50         60 
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE RRMHAKGSGA 

        70         80         90        100        110        120 
FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG AADAERDIRG FALKFYTEEG 

       130        140        150        160        170        180 
NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS 

       190        200        210        220        230        240 
DRGLPLSYRF VHGFGSHTYS FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS 

       250        260        270        280        290        300 
QRDLFEAIER GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN 

       310        320        330        340        350        360 
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH QIPVNAPKCP 

       370        380        390        400        410        420 
FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP LSIEGAADHW NHREDEDYFS 

       430        440        450        460        470        480 
QPRALYELLS DDEHQRMFAR IAGELSQASK ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG 


KDAK

« Hide

References

[1]"Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site."
Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J., Jouve H.-M., Hudry-Clergeon G.
J. Protein Chem. 14:59-72(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, MASS SPECTROMETRY.
Strain: PR.
[2]"Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH."
Gouet P., Jouve H.-M., Dideberg O.
J. Mol. Biol. 249:933-954(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Strain: PR.
[3]"Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy."
Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P., Nussaume L., Hajdu J.
Nat. Struct. Biol. 3:951-956(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), ABSORPTION SPECTROSCOPY.
[4]"High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron."
Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M.
Proteins 50:261-271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), EPR SPECTROSCOPY.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA58663.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E93X-ray2.00A1-484[»]
1H6NX-ray2.11A1-484[»]
1H7KX-ray2.40A2-484[»]
1M85X-ray2.00A1-484[»]
1MQFX-ray2.50A1-484[»]
1NM0X-ray2.30A1-484[»]
2CAGX-ray2.70A1-484[»]
2CAHX-ray2.70A1-484[»]
3HB6X-ray2.30A1-484[»]
ProteinModelPortalP42321.
SMRP42321. Positions 4-479.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP42321.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. Catalase_N. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP42321.

Entry information

Entry nameCATA_PROMI
AccessionPrimary (citable) accession number: P42321
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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